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#ATP synthesis

16 public questions tagged with this topic.

F-type ATPases differ from other ATPases because they:

F-type ATPases, historically termed FoF1 ATP synthases, represent an evolutionary unique class of rotary translocases that normally synthesize rather than consume ATP. While P-type and V-type pumps hydrolyze ATP to build H+ or Ca2+ gradients, F-type complexes harness pre-existing proton motive force created by electron transport chains in mitochondria, chloroplast thylakoids, and bacterial plasma membranes. The membrane-embedded Fo sector contains an oligomeric c-ring that binds protons via conserved carboxylate, rotating against subunit a as protons move down gradient. This rotation drives th

Ref: Stock et al., Curr Opin Struct Biol 2000, ATP synthase rotary mechanism; Alberts, Chapter 14.

F-class ATPases are primarily involved in:

F-type ATPases, often called ATP synthases, are evolutionarily related to V-type pumps but adapted for opposite physiological purpose in most contexts. Located in bacterial plasma membrane, mitochondrial inner membrane cristae and chloroplast thylakoid membrane, they consist of soluble F1 catalytic head containing alternating alpha and beta subunits around central gamma stalk and membrane embedded Fo base containing a subunit and c-ring proton channel. In respiring membranes electron transport complexes pump protons outward creating proton motive force combination of pH gradient and electrical

Ref: Boyer, Nobel Lecture 1997, F-Type ATP Synthase Rotary Mechanism and ATP Synthesis.